Ligand binding in the catalytic antibody 17E8. A free energy perturbation calculation study

Thomas Fox, Thomas S. Scanlan, Peter A. Kollman

Research output: Contribution to journalArticle

37 Scopus citations

Abstract

We present free energy calculations on the Michaelis complexes of the catalytic antibody 17E8 with two substrates, which differ only in their side chains. Replacing a -CH2- group with a -S- increases K(M) by a factor of about 5-8. This corresponds to a free energy 'preference' for the -CH2- ligand of about 0.9-1.3 kcal/mol. The calculations semiquantitatively reproduce the experimental free energies and show that the preference for a -CH2- over a -S- is mainly due to the more favorable solvation free energy in the unbound form of the molecule.

Original languageEnglish (US)
Pages (from-to)11571-11577
Number of pages7
JournalJournal of the American Chemical Society
Volume119
Issue number48
DOIs
StatePublished - Dec 1 1997

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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